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UCRIA_PEA
ID   UCRIA_PEA               Reviewed;         230 AA.
AC   P26291;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Cytochrome b6-f complex iron-sulfur subunit, chloroplastic;
DE            EC=7.1.1.6;
DE   AltName: Full=Plastohydroquinone:plastocyanin oxidoreductase iron-sulfur protein;
DE   AltName: Full=Rieske iron-sulfur protein;
DE            Short=ISP;
DE            Short=RISP;
DE   Flags: Precursor;
GN   Name=petC;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1421160; DOI=10.1007/bf00040617;
RA   Salter A.H., Newman B.J., Napier J.A., Gray J.C.;
RT   "Import of the precursor of the chloroplast Rieske iron-sulphur protein by
RT   pea chloroplasts.";
RL   Plant Mol. Biol. 20:569-574(1992).
CC   -!- FUNCTION: Component of the cytochrome b6-f complex, which mediates
CC       electron transfer between photosystem II (PSII) and photosystem I
CC       (PSI), cyclic electron flow around PSI, and state transitions.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinol + 2 H(+)(in) + 2 oxidized [plastocyanin] = a
CC         plastoquinone + 4 H(+)(out) + 2 reduced [plastocyanin];
CC         Xref=Rhea:RHEA:22148, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562,
CC         Rhea:RHEA-COMP:10039, Rhea:RHEA-COMP:10040, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17757, ChEBI:CHEBI:29036, ChEBI:CHEBI:49552,
CC         ChEBI:CHEBI:62192; EC=7.1.1.6;
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00628};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00628};
CC   -!- SUBUNIT: The 4 large subunits of the cytochrome b6-f complex are
CC       cytochrome b6, subunit IV (17 kDa polypeptide, petD), cytochrome f and
CC       the Rieske protein, while the 4 small subunits are petG, petL, petM and
CC       petN. The complex functions as a dimer (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Note=The
CC       transmembrane helix obliquely spans the membrane in one monomer, and
CC       its extrinsic C-terminal domain is part of the other monomer.
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: This protein is 1 of 2 subunits of the cytochrome b6-f
CC       complex that are encoded in the nucleus.
CC   -!- MISCELLANEOUS: The Rieske iron-sulfur protein is a high potential 2Fe-
CC       2S protein.
CC   -!- SIMILARITY: Belongs to the Rieske iron-sulfur protein family.
CC       {ECO:0000305}.
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DR   EMBL; X63605; CAA45151.1; -; mRNA.
DR   PIR; S26199; S26199.
DR   AlphaFoldDB; P26291; -.
DR   SMR; P26291; -.
DR   EnsemblPlants; Psat5g267960.1; Psat5g267960.1.cds; Psat5g267960.
DR   Gramene; Psat5g267960.1; Psat5g267960.1.cds; Psat5g267960.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; IEA:EnsemblPlants.
DR   GO; GO:0009496; F:plastoquinol--plastocyanin reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0010196; P:nonphotochemical quenching; IEA:EnsemblPlants.
DR   Gene3D; 2.102.10.10; -; 1.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR   InterPro; IPR014349; Rieske_Fe-S_prot.
DR   InterPro; IPR005805; Rieske_Fe-S_prot_C.
DR   PANTHER; PTHR10134; PTHR10134; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   PRINTS; PR00162; RIESKE.
DR   SUPFAM; SSF50022; SSF50022; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   2: Evidence at transcript level;
KW   2Fe-2S; Chloroplast; Disulfide bond; Electron transport; Iron; Iron-sulfur;
KW   Membrane; Metal-binding; Plastid; Thylakoid; Transit peptide; Translocase;
KW   Transmembrane; Transmembrane helix; Transport.
FT   TRANSIT         1..50
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000250"
FT   CHAIN           51..230
FT                   /note="Cytochrome b6-f complex iron-sulfur subunit,
FT                   chloroplastic"
FT                   /id="PRO_0000030691"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          115..213
FT                   /note="Rieske"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         157
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         159
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         175
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         178
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   DISULFID        162..177
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
SQ   SEQUENCE   230 AA;  24243 MW;  A60E42BC68048091 CRC64;
     MSSTTLSPTT PSQLCSGKSG ISCPSIALLV KPTRTQMTGR GNKGMKITCQ ATSIPADRVP
     DMSKRKTLNL LLLGALSLPT AGMLVPYGSF LVPPGSGSST GGTVAKDAVG NDVVATEWLK
     THAPGDRTLT QGLKGDPTYL VVEKDRTLAT FAINAVCTHL GCVVPFNQAE NKFICPCHGS
     QYNDQGRVVR GPAPLSLALA HCDVGVEDGK VVFVPWVETD FRTGDAPWWS
 
 
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